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P D Moens

Showing results (1-10 of 8) with videos related to

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Biochimica Et Biophysica Acta|March 14, 1995
Actin and the actomyosin interface: a reviewC G dos Remedios, P D Moens
Biochemistry|June 17, 1997
A conformational change in F-actin when myosin binds: fluorescence resonance energy transfer detects an increase in the radial coordinate of Cys-374P D Moens, C G dos Remedios
Journal of Structural Biology|September 1, 1995
Fluorescence resonance energy transfer spectroscopy is a reliable "ruler" for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factorC G dos Remedios, P D Moens
Journal of Muscle Research and Cell Motility|February 1, 1996
Lack of myoblasts migration between transplanted and host muscles of mdx and normal miceP D Moens, M C Van-Schoor, G Maréchal
Biochemistry|November 8, 1994
Determination of the radial coordinate of Cys-374 in F-actin using fluorescence resonance energy transfer spectroscopy: effect of phalloidin on polymer assemblyP D Moens, D J Yee, C G dos Remedios
The Biochemical Journal|July 15, 1996
Structural changes in subdomain 2 of G-actin observed by fluorescence spectroscopyJ Moraczewska, H Strzelecka-Gołaszewska, P D Moens, et al.
Biophysical Journal|July 1, 1996
Distance measurements near the myosin head-rod junction using fluorescence spectroscopyM Kekic, W Huang, P D Moens, et al.
Calcified Tissue International|December 1, 1993
Spectrum decomposition through maximum likelihood common factor analysis of the EPR spectra of Na+ containing carbonated apatites dried at 400 degrees CP D Moens, R M Verbeeck, P J De Volder, et al.
Pageof 1

Showing results (1-10 of 8) with videos related to

Sort By:
Pageof 1
Biochimica Et Biophysica Acta|March 14, 1995
Actin and the actomyosin interface: a reviewC G dos Remedios, P D Moens
Biochemistry|June 17, 1997
A conformational change in F-actin when myosin binds: fluorescence resonance energy transfer detects an increase in the radial coordinate of Cys-374P D Moens, C G dos Remedios
Journal of Structural Biology|September 1, 1995
Fluorescence resonance energy transfer spectroscopy is a reliable "ruler" for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factorC G dos Remedios, P D Moens
Journal of Muscle Research and Cell Motility|February 1, 1996
Lack of myoblasts migration between transplanted and host muscles of mdx and normal miceP D Moens, M C Van-Schoor, G Maréchal
Biochemistry|November 8, 1994
Determination of the radial coordinate of Cys-374 in F-actin using fluorescence resonance energy transfer spectroscopy: effect of phalloidin on polymer assemblyP D Moens, D J Yee, C G dos Remedios
The Biochemical Journal|July 15, 1996
Structural changes in subdomain 2 of G-actin observed by fluorescence spectroscopyJ Moraczewska, H Strzelecka-Gołaszewska, P D Moens, et al.
Biophysical Journal|July 1, 1996
Distance measurements near the myosin head-rod junction using fluorescence spectroscopyM Kekic, W Huang, P D Moens, et al.
Calcified Tissue International|December 1, 1993
Spectrum decomposition through maximum likelihood common factor analysis of the EPR spectra of Na+ containing carbonated apatites dried at 400 degrees CP D Moens, R M Verbeeck, P J De Volder, et al.
Pageof 1